Protein Stability Attractive Vander Waals forces occur between polar molecules in the solid state apolar molecules in the liquid state any pair of nearby atoms only if other forces are less favorable polar molecules in the solid state apolar molecules in the liquid state any pair of nearby atoms only if other forces are less favorable ANSWER DOWNLOAD EXAMIANS APP
Protein Stability The correlation between free energy ΔG transfer between the aqueous/organic phases and the surface area of amino acid residues ignores the important contribution of the peptide bond is similar to effects seen with SDS denaturation reflects the reduction in solvent-accessible area during protein folding is only meaningful for the polar amino acids ignores the important contribution of the peptide bond is similar to effects seen with SDS denaturation reflects the reduction in solvent-accessible area during protein folding is only meaningful for the polar amino acids ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Buried hydrophobic side chains in a globular protein fit into a hole formed by the side chains of 13-15 other amino acids 9-12 other amino acids 1-3 other amino acids 5-7 other amino acids 13-15 other amino acids 9-12 other amino acids 1-3 other amino acids 5-7 other amino acids ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Which of the following is the most correct? Charged amino acids are seldom buried in the interior of a protein Charged amino acids are never buried in the interior of a protein Tyrosine is only found in the interior of proteins All hydrophobic amino acids are buried when a protein folds Charged amino acids are seldom buried in the interior of a protein Charged amino acids are never buried in the interior of a protein Tyrosine is only found in the interior of proteins All hydrophobic amino acids are buried when a protein folds ANSWER DOWNLOAD EXAMIANS APP
Protein Stability If the egg white protein, ovalbumin, is denatured in a hard-boiled egg, then which of the following is least affected? The primary structure of ovalbumin The secondary structure of ovalbumin The quaternary structure of ovalbumin The tertiary structure of ovalbumin The primary structure of ovalbumin The secondary structure of ovalbumin The quaternary structure of ovalbumin The tertiary structure of ovalbumin ANSWER DOWNLOAD EXAMIANS APP
Protein Stability Since ΔG° = -RTlnK a 10-fold increase in K decreases ΔG° by about 2.3*RT a 10-fold increase in K decreases ΔG° by about 10-fold a 10-fold decrease in K increases ΔG° by about 10-fold a 10-fold decrease in K decreases ΔG° by about 2.3*RT a 10-fold increase in K decreases ΔG° by about 2.3*RT a 10-fold increase in K decreases ΔG° by about 10-fold a 10-fold decrease in K increases ΔG° by about 10-fold a 10-fold decrease in K decreases ΔG° by about 2.3*RT ANSWER DOWNLOAD EXAMIANS APP
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